Isolation of a protease from sea urchin eggs before and after fertilization

Upon fertilization, sea urchin eggs (Stronglyocentrotus pupuratus) release a protease into the surrounding sea water. This protease is in a particulate form which can be solubilized. The soluble form was purified by affinity chromatography on columns of immobilized soybean trypsin inhibitor. The pur...

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Bibliographic Details
Published in:Biochemistry (Easton) 1975-11, Vol.14 (22), p.4923-4927
Main Authors: Fodor, Eric J. B, Ako, Harry, Walsh, Kenneth A
Format: Article
Language:English
Subjects:
Animals
Chromatography, Affinity
Female
Fertilization
Male
Molecular Weight
Ovum - enzymology
Peptide Hydrolases - isolation & purification
Peptide Hydrolases - metabolism
Sea Urchins
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Summary:Upon fertilization, sea urchin eggs (Stronglyocentrotus pupuratus) release a protease into the surrounding sea water. This protease is in a particulate form which can be solubilized. The soluble form was purified by affinity chromatography on columns of immobilized soybean trypsin inhibitor. The purified enzyme is similar to bovine trypsin both in molecular weight (22500) and in susceptibility to inhibitors such as diisopropyl phosphofluoridate and soybean trypsin inhibitor. In contrast, extracts of unfertilized eggs appear to contain an inactive form of the enzyme which can be activated by dialysis at pH 4.6. The enzyme, as purified from extracts activated in this manner, was similar in its properties to that from fertilized eggs.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00693a022